2BBZ,3CL3


Conserved Protein Domain Family
DED_Caspase-like_r1

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cd08776: DED_Caspase-like_r1 
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Death effector domain, repeat 1, of initator caspase-like proteins
Death Effector Domain (DED), first repeat, found in initator caspase-like proteins, like caspase-8 and -10 and c-FLIP. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of DISC. All members contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Statistics
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PSSM-Id: 176754
View PSSM: cd08776
Aligned: 3 rows
Threshold Bit Score: 86.4215
Threshold Setting Gi: 190613686
Created: 18-Feb-2010
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
DED1/DED2charge triad
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:DED1/DED2 interface [polypeptide binding site]
Evidence:
  • Comment:Based on the structure of the tandem DED domains of v-FLIP.
  • Comment:The tandem DED domains, DED1 and DED2, in FLIP are associated rigidly to form a single compact structure, with each domain playing a unique structural role and is not interchangeable with the other. This explains why both domains are required for FLIP function.
  • Structure:2BBZ_A; Interface between DED1 and DED2 in Molluscum contagiosum virus MC159 (v-FLIP); contacts at 4A.
    View structure with Cn3D
  • Structure:3CL3_A; Interface between DED1 and DED2 domains in Human herpesvirus 8 v-FLIP; contacts at 4A.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                     ##   #  ## ##                                   #   #           
2BBZ_A         9 SLPFLRHLLEELDSHEDSLLLFLCHDAAPGCTTv-----TQALCSLSQQRKL---TLAALVEMLYVLqRMDLLKSRF 77  McVI
NP_001038154   5 FRKLLFDISEALATEELAALKFLSLEHVPVRKQedteepKAFFEVLKEKGMIeveDLFFLKELLYRInRIDLLASHL 81  chicken
3CL3_A         8 TYEVLCEVARKLGTDDREVVLFLLNVFIPQPTLaq---lIGALRALKEEGRL---TFPLLAECLFRAgRRDLLRDLL 78  KSHV

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